First and Last Name/s of Presenters

Nicholas FuscoFollow

Participation Type

Poster

Title of Poster or Paper

Peptide-Functionalized Magnetically-Active Nanoparticles for Targeted Manipulation of Amyloid Fibrils

Mentor/s

Dr. Benjamin Alper, Chemistry Department

Location

University Commons

Start Day/Time

4-20-2018 1:00 PM

End Day/Time

4-20-2018 3:00 PM

Abstract

The amyloid hypothesis asserts that accumulation of amyloid beta (Aβ) peptides is a primary cause of Alzheimer’s disease. This project seeks to identify novel strategies for disruption or elimination of amyloid fibrils through development of peptide-functionalized magnetically-active nanoparticles. Water-soluble polyethylene oxide-stabilized iron oxide nanoparticles (PEO-IONPs) were conjugated through azide “click” chemistry to short, hydrophobic KLVFFAL peptides approximating the minimal sufficient Aβ peptide fibril nucleation motif (i.e., yielding KLVFFAL-PEO-IONPs). Experimental efforts sought to incorporate this particle within elongating amyloid fibrils, with peptide aggregation assessed by thioflavin T fluorescence assay. Amyloid peptide aggregation was observed in the presence and in the absence of KLVFFAL-PEO-IONPs. Preliminary data suggest that amyloid fibril partitioning was achieved in the presence of KLVFFAL-PEO-IONPs subject to application of a magnetic field.

College

College of Arts and Sciences

College and Major available

Chemistry

Creative Commons License

Creative Commons Attribution-Noncommercial 4.0 License
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Apr 20th, 1:00 PM Apr 20th, 3:00 PM

Peptide-Functionalized Magnetically-Active Nanoparticles for Targeted Manipulation of Amyloid Fibrils

University Commons

The amyloid hypothesis asserts that accumulation of amyloid beta (Aβ) peptides is a primary cause of Alzheimer’s disease. This project seeks to identify novel strategies for disruption or elimination of amyloid fibrils through development of peptide-functionalized magnetically-active nanoparticles. Water-soluble polyethylene oxide-stabilized iron oxide nanoparticles (PEO-IONPs) were conjugated through azide “click” chemistry to short, hydrophobic KLVFFAL peptides approximating the minimal sufficient Aβ peptide fibril nucleation motif (i.e., yielding KLVFFAL-PEO-IONPs). Experimental efforts sought to incorporate this particle within elongating amyloid fibrils, with peptide aggregation assessed by thioflavin T fluorescence assay. Amyloid peptide aggregation was observed in the presence and in the absence of KLVFFAL-PEO-IONPs. Preliminary data suggest that amyloid fibril partitioning was achieved in the presence of KLVFFAL-PEO-IONPs subject to application of a magnetic field.